O87545
Gene name |
gyrB |
Protein name |
DNA gyrase subunit B |
Names |
|
Species |
Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104) |
KEGG Pathway |
tde:TDE_0002 |
EC number |
5.6.2.2: Enzymes altering nucleic acid conformation |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O87545
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O87545-F1 | Predicted | AlphaFoldDB |
No variants for O87545
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O87545 | |||||
No associated diseases with O87545
6 regional properties for O87545
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DNA gyrase B subunit, C-terminal | 568 - 628 | IPR002288 |
| domain | Histidine kinase/HSP90-like ATPase | 31 - 175 | IPR003594 |
| domain | TOPRIM domain | 423 - 537 | IPR006171 |
| domain | DNA topoisomerase, type IIA, subunit B, domain 2 | 223 - 395 | IPR013506 |
| conserved_site | DNA topoisomerase, type IIA, conserved site | 427 - 435 | IPR018522 |
| domain | DNA gyrase subunit B, TOPRIM domain | 423 - 536 | IPR034160 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.2.2 | Enzymes altering nucleic acid conformation |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromosome | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA topological change | The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number. |
| DNA-templated DNA replication | A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTKSNYSANN | ITVLKGLEAV | RKRPGMYIGS | TGPDGLHHLV | YEVVDNCIDE | AMAGFCDKIL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVLEPNDIVR | VEDNGRGIPV | DIHPTEKISA | LELVLTRLHA | GGKFDKGSYK | VSGGLHGVGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SVVNALSVWM | EAKVYKDGFE | HYAKFEKGSI | LEPVKKIGET | EKSGTVIRWA | VDPSIFTETT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VYNFEVLATR | LRELAFLNSK | ISITMRDERL | STPKEVTFAF | EGGISQFVSY | LNESKQVFPK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SPVFIEGEKN | DILCEVAIQY | NDGYNENLLS | FVNDINTREG | GTHLEGFKTA | LTRVMNDFLK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KYPKLVKKMD | KEEKLTGEDV | RAGLTAIVSV | KVPEPQFEGQ | TKTKLGNSDV | RGIVDSFVNE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLTLFFEQNP | NEVEKVLEKC | VAEAAARIAA | RRAKEATRRK | SGLDSFGLPG | KLADCSLKDP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ESCEVYIVEG | DSAGGSAKKG | RDSKTQAILP | LWGKMLNVEK | TRLDKVVNNE | KLQPIIATLG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TGIGKDFNIE | KLRYHKVIIM | ADADVDGSHI | RTLLLTFFFR | YMPQVIEKGH | VYLAMPPLYK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ISHNKKEWYV | YNDDERDSVL | DQIGRGNNAA | VQRYKGLGEM | DGTQLWETTM | DPARRKMMRV |
| 610 | 620 | 630 | |||
| TLPDAVEADR | IFSTLMGEEV | EPRRKFIEEN | AVYANLDV |